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Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform (PP2A subunit B isoform B55-beta) (PP2A subunit B isoform PR55-beta) (PP2A subunit B isoform R2-beta) (PP2A subunit B isoform beta)

 2ABB_MOUSE              Reviewed;         443 AA.
Q6ZWR4; Q3UF60; Q8K413; Q9D3B7; Q9D6I1;
24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
05-JUL-2004, sequence version 1.
28-MAR-2018, entry version 117.
RecName: Full=Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform;
AltName: Full=PP2A subunit B isoform B55-beta;
AltName: Full=PP2A subunit B isoform PR55-beta;
AltName: Full=PP2A subunit B isoform R2-beta;
AltName: Full=PP2A subunit B isoform beta;
Name=Ppp2r2b;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=CD-1, and Czech II; TISSUE=Lung tumor, and Testis;
PubMed=12473071; DOI=10.1046/j.1460-9568.2002.02274.x;
Schmidt K., Kins S., Schild A., Nitsch R.M., Hemmings B.A., Goetz J.;
"Diversity, developmental regulation and distribution of murine PR55/B
subunits of protein phosphatase 2A.";
Eur. J. Neurosci. 16:2039-2048(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J;
TISSUE=Hippocampus, Medulla oblongata, Spinal cord, and
Sympathetic ganglion;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J, and Czech II; TISSUE=Brain, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
-!- FUNCTION: The B regulatory subunit might modulate substrate
selectivity and catalytic activity, and also might direct the
localization of the catalytic enzyme to a particular subcellular
compartment. Within the PP2A holoenzyme complex, isoform 2 is
required to promote proapoptotic activity. Isoform 2 regulates
neuronal survival through the mitochondrial fission and fusion
balance. {ECO:0000250}.
-!- SUBUNIT: PP2A consists of a common heterodimeric core enzyme,
composed of a 36 kDa catalytic subunit (subunit C) and a 65 kDa
constant regulatory subunit (PR65 or subunit A), that associates
with a variety of regulatory subunits. Proteins that associate
with the core dimer include three families of regulatory subunits
B (the R2/B/PR55/B55, R3/B''/PR72/PR130/PR59 and R5/B'/B56
families), the 48 kDa variable regulatory subunit, viral proteins,
and cell signaling molecules (By similarity). Interacts with
TOMM22 (By similarity). Interacts with IER5 (via N- and C-terminal
regions) (By similarity). {ECO:0000250,
ECO:0000250|UniProtKB:P36877, ECO:0000250|UniProtKB:Q00005}.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm. Cytoplasm,
cytoskeleton. Membrane.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000250}.
Mitochondrion {ECO:0000250}. Mitochondrion outer membrane
{ECO:0000250}. Note=Under basal conditions, localizes to both
cytosolic and mitochondrial compartments. Relocalizes from the
cytosolic to the mitochondrial compartment during apoptosis. Its
targeting to the outer mitochondrial membrane (OMM) involves an
association with import receptors of the TOM complex and is
required to promote proapoptotic activity (By similarity).
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1; Synonyms=Bbeta;
IsoId=Q6ZWR4-1; Sequence=Displayed;
Name=2; Synonyms=Bbeta2;
IsoId=Q6ZWR4-2; Sequence=VSP_037983;
Note=Contains a cryptic mitochondrial transit peptide at
positions 1-26. {ECO:0000250};
Name=3; Synonyms=Bbeta1;
IsoId=Q6ZWR4-3; Sequence=VSP_037982;
-!- TISSUE SPECIFICITY: Expressed in brain, testis, lung and spleen.
In the brain, expressed in the cortex, hippocampus and cerebellum
(at protein level). {ECO:0000269|PubMed:12473071}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo at 14 and 17 dpc.
{ECO:0000269|PubMed:12473071}.
-!- DOMAIN: The N-terminal 26 residues of isoform 2 constitute a
cryptic mitochondrial matrix import signal with critical basic and
hydrophobic residues, that is necessary and sufficient for
targeting the PP2A holoenzyme to the outer mitochondrial membrane
(OMM) and does not affect holoenzyme formation or catalytic
activity. {ECO:0000250}.
-!- DOMAIN: The last WD repeat of isoform 2 constitutes a
mitochondrial stop-transfer domain that confers resistance to the
unfolding step process required for import and therefore prevents
PPP2R2B matrix translocation and signal sequence cleavage.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the phosphatase 2A regulatory subunit B
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAB31079.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
Sequence=EDL10024.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF512670; AAM46987.1; -; mRNA.
EMBL; AF536771; AAN05641.1; -; mRNA.
EMBL; AK013600; BAB28921.1; -; mRNA.
EMBL; AK018119; BAB31079.1; ALT_SEQ; mRNA.
EMBL; AK039592; BAC30395.1; -; mRNA.
EMBL; AK148956; BAE28701.1; -; mRNA.
EMBL; CH466528; EDL10024.1; ALT_SEQ; Genomic_DNA.
EMBL; CH466528; EDL10025.1; -; Genomic_DNA.
EMBL; BC026686; AAH26686.1; -; mRNA.
EMBL; BC088979; AAH88979.1; -; mRNA.
CCDS; CCDS29216.1; -. [Q6ZWR4-2]
RefSeq; NP_082668.1; NM_028392.3. [Q6ZWR4-2]
UniGene; Mm.26134; -.
ProteinModelPortal; Q6ZWR4; -.
SMR; Q6ZWR4; -.
BioGrid; 215651; 2.
CORUM; Q6ZWR4; -.
IntAct; Q6ZWR4; 1.
STRING; 10090.ENSMUSP00000025377; -.
iPTMnet; Q6ZWR4; -.
PhosphoSitePlus; Q6ZWR4; -.
PaxDb; Q6ZWR4; -.
PeptideAtlas; Q6ZWR4; -.
PRIDE; Q6ZWR4; -.
Ensembl; ENSMUST00000025377; ENSMUSP00000025377; ENSMUSG00000024500. [Q6ZWR4-2]
Ensembl; ENSMUST00000117687; ENSMUSP00000113731; ENSMUSG00000024500. [Q6ZWR4-1]
Ensembl; ENSMUST00000120632; ENSMUSP00000113411; ENSMUSG00000024500. [Q6ZWR4-1]
GeneID; 72930; -.
KEGG; mmu:72930; -.
UCSC; uc008eub.2; mouse. [Q6ZWR4-1]
UCSC; uc008euc.2; mouse. [Q6ZWR4-2]
CTD; 5521; -.
MGI; MGI:1920180; Ppp2r2b.
eggNOG; KOG1354; Eukaryota.
eggNOG; COG5170; LUCA.
GeneTree; ENSGT00390000006311; -.
HOGENOM; HOG000089745; -.
HOVERGEN; HBG000012; -.
InParanoid; Q6ZWR4; -.
KO; K04354; -.
OMA; YSNAHAY; -.
OrthoDB; EOG091G09BB; -.
TreeFam; TF105553; -.
PRO; PR:Q6ZWR4; -.
Proteomes; UP000000589; Chromosome 18.
Bgee; ENSMUSG00000024500; -.
Genevisible; Q6ZWR4; MM.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0000159; C:protein phosphatase type 2A complex; IBA:GO_Central.
GO; GO:0019888; F:protein phosphatase regulator activity; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0032502; P:developmental process; IBA:GO_Central.
GO; GO:0000278; P:mitotic cell cycle; IBA:GO_Central.
GO; GO:0070262; P:peptidyl-serine dephosphorylation; IBA:GO_Central.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR000009; PP2A_PR55.
InterPro; IPR018067; PP2A_PR55_CS.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR036322; WD40_repeat_dom_sf.
PANTHER; PTHR11871; PTHR11871; 1.
PIRSF; PIRSF037309; PP2A_PR55; 1.
PRINTS; PR00600; PP2APR55.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 3.
PROSITE; PS01024; PR55_1; 1.
PROSITE; PS01025; PR55_2; 1.
PROSITE; PS00678; WD_REPEATS_1; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Cytoplasm;
Cytoskeleton; Membrane; Mitochondrion; Mitochondrion outer membrane;
Phosphoprotein; Reference proteome; Repeat; WD repeat.
CHAIN 1 443 Serine/threonine-protein phosphatase 2A
55 kDa regulatory subunit B beta isoform.
/FTId=PRO_0000071423.
REPEAT 22 61 WD 1.
REPEAT 87 128 WD 2.
REPEAT 171 209 WD 3.
REPEAT 220 260 WD 4.
REPEAT 279 317 WD 5.
REPEAT 334 375 WD 6.
REPEAT 410 442 WD 7.
MOD_RES 275 275 Phosphoserine.
{ECO:0000250|UniProtKB:P36877}.
MOD_RES 295 295 Phosphotyrosine.
{ECO:0000250|UniProtKB:P36877}.
MOD_RES 298 298 Phosphothreonine.
{ECO:0000250|UniProtKB:P36877}.
VAR_SEQ 1 24 MEEDIDTRKINNSFLRDHSYATEA -> MKPFTA (in
isoform 3).
{ECO:0000303|PubMed:12473071}.
/FTId=VSP_037982.
VAR_SEQ 1 21 MEEDIDTRKINNSFLRDHSYA -> MKCFSRYLPYIFRPPN
TILSSSCH (in isoform 2).
{ECO:0000303|PubMed:12473071,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_037983.
CONFLICT 35 35 T -> S (in Ref. 2; BAE28701).
{ECO:0000305}.
SEQUENCE 443 AA; 51710 MW; C383C834B2852B8F CRC64;
MEEDIDTRKI NNSFLRDHSY ATEADIISTV EFNHTGELLA TGDKGGRVVI FQREQESKNQ
VHRRGEYNVY STFQSHEPEF DYLKSLEIEE KINKIRWLPQ QNAAYFLLST NDKTVKLWKV
SERDKRPEGY NLKDEEGRLR DPATITTLRV PVLRPMDLMV EATPRRVFAN AHTYHINSIS
VNSDYETYMS ADDLRINLWN FEITNQSFNI VDIKPANMEE LTEVITAAEF HPHHCNTFVY
SSSKGTIRLC DMRASALCDR HTKFFEEPED PSNRSFFSEI ISSISDVKFS HSGRYIMTRD
YLTVKVWDLN MENRPIETYQ VHDYLRSKLC SLYENDCIFD KFECVWNGSD SVIMTGSYNN
FFRMFDRNTK RDVTLEASRE NSKPRAILKP RKVCVGGKRR KDEISVDSLD FSKKILHTAW
HPSENIIAVA ATNNLYIFQD KVN


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